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[PMID]:29289926
[Au] Autor:Josse G; Douki T; Le Digabel J; Gravier E; Questel E
[Ad] Endereço:Centre de Recherche sur la Peau, Pierre Fabre Dermo-Cosmétique, F-31000 Toulouse, France. Electronic address: gwendal.josse@pierre-fabre.com.
[Ti] Título:The use of suction blisters to measure sunscreen protection against UVR-induced DNA damage.
[So] Source:J Photochem Photobiol B;179:1-6, 2018 Feb.
[Is] ISSN:1873-2682
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:The formation of DNA photoproducts caused by solar UVR exposure needs to be investigated in-vivo and in particular in order to assess sunscreens' level of protection against solar genotoxicity. The study's purposes were: i) to evaluate if the roof of suction blisters is an appropriate sampling method for measuring photoproducts, and ii) to measure in-vivo sunscreen protection against cyclobutane pyrimidine dimers. Skin areas on the interior forearms of eight healthy volunteers were exposed in-vivo to 2 MED of simulated solar radiation (SSR) and to 15 MED on a sunscreen protected area. After irradiation, six suction blisters were induced and the blister roofs were collected. Analysis of SSR-induced CPDs was performed by two independent methods: a chromatography coupled to mass spectroscopy (HPLC-MS/MS) approach and a 3D-imaging of CPD immunostaining by multiphoton microscopy on floating epidermal sheets. HPLC-MS/MS analyses showed that SSR-unexposed skin presented no CPD dimers, whereas 2 MED SSR-exposed skin showed a significant number of TT-CPD. The sunscreen covered skin exposed to 15 MED appeared highly protected from DNA damage, as the amount of CPD-dimers remained below the detection limit. The multiphoton-immunostaining analysis consistently showed that no CPD staining was observed on the non-SSR-exposed skin. A significant increase of CPD staining intensity and number of CPD-positive cells were observed on the 2 MED SSR-exposed skin. Sunscreen protected skin presented a very low staining intensity and the number of CPD-positive cells remained very close to non-SSR-exposed skin. This study showed that suction blister samples are very appropriate for measuring CPD dimers in-vivo, and that sunscreens provide high protection against UVR-induced DNA damage.
[Mh] Termos MeSH primário: Dano ao DNA/efeitos dos fármacos
Pele/efeitos dos fármacos
Protetores Solares/farmacologia
Raios Ultravioleta
[Mh] Termos MeSH secundário: Adulto
Vesícula/genética
Vesícula/metabolismo
Vesícula/patologia
Cromatografia Líquida de Alta Pressão
Dano ao DNA/efeitos da radiação
Feminino
Seres Humanos
Masculino
Dímeros de Pirimidina/análise
Pele/efeitos da radiação
Fator de Proteção Solar
Espectrometria de Massas em Tandem
Adulto Jovem
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Pyrimidine Dimers); 0 (Sunscreening Agents)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180223
[Lr] Data última revisão:
180223
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180101
[St] Status:MEDLINE


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[PMID]:29275239
[Au] Autor:Singh J; Srivastva AK; Mandal P; Chandra S; Dubey D; Dwivedi A; Chopra D; Tripathi A; Ray RS
[Ad] Endereço:Photobiology Laboratory, Systems Toxicology and Health Risk Assessment Group, CSIR-Indian Institute of Toxicology Research (CSIR-IITR), Vishvigyan Bhavan, 31, Mahatma Gandhi Marg, Lucknow 226001, Uttar Pradesh, India; Academy of Scientific and Innovative Research (AcSIR), CSIR-IITR Campus, Lucknow,
[Ti] Título:Under ambient UVA exposure, pefloxacin exhibits both immunomodulatory and genotoxic effects via multiple mechanisms.
[So] Source:J Photochem Photobiol B;178:593-605, 2018 Jan.
[Is] ISSN:1873-2682
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:Pefloxacin (PFLX) is an antibiotic, which shows broad spectrum antimicrobial activities. It is an important derivative of fluoroquinolones (FLQs) group. Ultraviolet radiation (200-400nm) causes major problem for living being which comes at the earth surface naturally through sunlight and increasing regularly due to ozone depletion. PFLX was photodegraded in 5h and forms photoproduct under UVA exposure. At the non photocytotoxic dose PFLX, shows reduced phagocytosis activity, NO (nitric oxide) production, large vacuole formation and down regulated IL-6, TNF-α and IL-1 in BALB/c macrophages at both genes and proteins levels. At higher doses (photocytotoxic doses), PFLX induced a concentration dependent decrease in cell viability of human keratinocyte cell line (HaCaT) and peritoneal macrophages of BALB/c mice. Our molecular docking suggests that PFLX binds only to the cleaved DNA in the DNA-human TOP2A complex. Topoisomerase assay confirmed that PFLX inhibits human topoisomerase by forming an adduct with DNA. Photosensitized PFLX also caused intracellular ROS mediated DNA damage and formation of micronuclei and cyclobutane pyrimidine dimers (CPDs). Increase intracellular ROS leads to apoptosis which was proved through lysosomal destabilization and reduced mitochondrial membrane potential (MMP). Our present study shows that ambient UVA exposure in the presence of PFLX caused immunomodulatory as well as photogenotoxic effects. Therefore, patients under PFLX drug treatment should avoid sunlight exposure, especially during peak hours for their photosafety.
[Mh] Termos MeSH primário: Dano ao DNA/efeitos dos fármacos
Pefloxacina/química
Fármacos Fotossensibilizantes/química
Raios Ultravioleta
[Mh] Termos MeSH secundário: Animais
Apoptose/efeitos dos fármacos
Apoptose/efeitos da radiação
Sítios de Ligação
Pontos de Checagem do Ciclo Celular/efeitos dos fármacos
Pontos de Checagem do Ciclo Celular/efeitos da radiação
Células Cultivadas
DNA/química
DNA/metabolismo
Dano ao DNA/efeitos da radiação
DNA Topoisomerases Tipo II/química
DNA Topoisomerases Tipo II/metabolismo
Feminino
Seres Humanos
Interleucina-6/genética
Interleucina-6/metabolismo
Macrófagos/citologia
Macrófagos/efeitos dos fármacos
Macrófagos/metabolismo
Macrófagos/efeitos da radiação
Potencial da Membrana Mitocondrial/efeitos dos fármacos
Potencial da Membrana Mitocondrial/efeitos da radiação
Camundongos
Simulação de Acoplamento Molecular
Pefloxacina/toxicidade
Fármacos Fotossensibilizantes/toxicidade
Proteínas de Ligação a Poli-ADP-Ribose/química
Proteínas de Ligação a Poli-ADP-Ribose/metabolismo
Dímeros de Pirimidina/análise
Espécies Reativas de Oxigênio/metabolismo
Fator de Necrose Tumoral alfa/genética
Fator de Necrose Tumoral alfa/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Interleukin-6); 0 (Photosensitizing Agents); 0 (Poly-ADP-Ribose Binding Proteins); 0 (Pyrimidine Dimers); 0 (Reactive Oxygen Species); 0 (Tumor Necrosis Factor-alpha); 2H52Z9F2Q5 (Pefloxacin); 9007-49-2 (DNA); EC 5.99.1.3 (DNA Topoisomerases, Type II); EC 5.99.1.3 (TOP2A protein, human)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180212
[Lr] Data última revisão:
180212
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171225
[St] Status:MEDLINE


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[PMID]:29283335
[Au] Autor:Pudroma X; Duoji G; Grigalavicius M; Jie D; Juzeniene A
[Ad] Endereço:Department of Physics, Tibet University, Lhasa, China.
[Ti] Título:Molecular Mechanisms of UVA-Induced Melanoma.
[So] Source:J Environ Pathol Toxicol Oncol;36(3):217-228, 2017.
[Is] ISSN:2162-6537
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Cutaneous melanoma is a deadly skin cancer, resulting from malignant transformation of melanocytes. Long-wave ultraviolet radiation (315-400 nm) is able to damage DNA, cause mutations, and induce melanoma. However, the exact mechanisms of UVA-induced cutaneous melanoma remain a matter of debate. In this review, we give a brief characterization of the most important elements in the photobiology of UVA in melanomagenesis.
[Mh] Termos MeSH primário: Melanoma/etiologia
Neoplasias Induzidas por Radiação/etiologia
Neoplasias Cutâneas/etiologia
Raios Ultravioleta
[Mh] Termos MeSH secundário: Dano ao DNA
Feminino
Seres Humanos
Masculino
Melaninas/química
Dímeros de Pirimidina/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Melanins); 0 (Pyrimidine Dimers)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180104
[Lr] Data última revisão:
180104
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171229
[St] Status:MEDLINE
[do] DOI:10.1615/JEnvironPatholToxicolOncol.2017020213


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[PMID]:28981631
[Au] Autor:Han C; Zhao R; Kroger J; He J; Wani G; Wang QE; Wani AA
[Ad] Endereço:Department of Radiology.
[Ti] Título:UV radiation-induced SUMOylation of DDB2 regulates nucleotide excision repair.
[So] Source:Carcinogenesis;38(10):976-985, 2017 Oct 01.
[Is] ISSN:1460-2180
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Subunit 2 of DNA damage-binding protein complex (DDB2) is an early sensor of nucleotide excision repair (NER) pathway for eliminating DNA damage induced by UV radiation (UVR) and cisplatin treatments of mammalian cells. DDB2 is modified by ubiquitin and poly(ADP-ribose) (PAR) in response to UVR, and these modifications play a crucial role in regulating NER. Here, using immuno-analysis of irradiated cell extracts, we have identified multiple post-irradiation modifications of DDB2 protein. Interestingly, although the DNA lesions induced by both UVR and cisplatin are corrected by NER, only the UV irradiation, but not the cisplatin treatment, induces any discernable DDB2 modifications. We, for the first time, show that the appearance of UVR-induced DDB2 modifications depend on the binding of DDB2 to the damaged chromatin and the participation of functionally active 26S proteasome. The in vitro and in vivo analysis revealed that SUMO-1 conjugations comprise a significant portion of these UVR-induced DDB2 modifications. Mapping of SUMO-modified sites demonstrated that UVR-induced SUMOylation occurs on Lys-309 residue of DDB2 protein. Mutation of Lys-309 to Arg-309 diminished the DDB2 SUMOylation observable both in vitro and in vivo. Moreover, K309R mutated DDB2 lost its function of recruiting XPC to the DNA damage sites, as well as the ability to repair cyclobutane pyrimidine dimers following cellular UV irradiation. Taken together, our results indicate that DDB2 is modified by SUMOylation upon UV irradiation, and this post-translational modification plays an important role in the initial recognition and processing of UVR-induced DNA damage occurring within the context of chromatin.
[Mh] Termos MeSH primário: Reparo do DNA/efeitos da radiação
Proteínas de Ligação a DNA/metabolismo
Sumoilação/efeitos da radiação
[Mh] Termos MeSH secundário: Cromatina/metabolismo
Cromatina/efeitos da radiação
Cisplatino/farmacologia
Reparo do DNA/efeitos dos fármacos
Reparo do DNA/fisiologia
Proteínas de Ligação a DNA/genética
Células HeLa
Seres Humanos
Lisina/metabolismo
Complexo de Endopeptidases do Proteassoma/metabolismo
Dímeros de Pirimidina/genética
Dímeros de Pirimidina/metabolismo
Sumoilação/efeitos dos fármacos
Raios Ultravioleta
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Chromatin); 0 (DDB2 protein, human); 0 (DNA-Binding Proteins); 0 (Pyrimidine Dimers); 156533-34-5 (XPC protein, human); EC 3.4.25.1 (Proteasome Endopeptidase Complex); EC 3.4.99.- (ATP dependent 26S protease); K3Z4F929H6 (Lysine); Q20Q21Q62J (Cisplatin)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171030
[Lr] Data última revisão:
171030
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171006
[St] Status:MEDLINE
[do] DOI:10.1093/carcin/bgx076


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[PMID]:28802828
[Au] Autor:Zhang M; Wang L; Zhong D
[Ad] Endereço:Department of Physics, Department of Chemistry and Biochemistry, Programs of Biophysics, Chemical Physics, and Biochemistry, The Ohio State University, Columbus, OH 43210, USA.
[Ti] Título:Photolyase: Dynamics and electron-transfer mechanisms of DNA repair.
[So] Source:Arch Biochem Biophys;632:158-174, 2017 Oct 15.
[Is] ISSN:1096-0384
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Photolyase, a flavoenzyme containing flavin adenine dinucleotide (FAD) molecule as a catalytic cofactor, repairs UV-induced DNA damage of cyclobutane pyrimidine dimer (CPD) and pyrimidine-pyrimidone (6-4) photoproduct using blue light. The FAD cofactor, conserved in the whole protein superfamily of photolyase/cryptochromes, adopts a unique folded configuration at the active site that plays a critical functional role in DNA repair. Here, we review our comprehensive characterization of the dynamics of flavin cofactor and its repair photocycles by different classes of photolyases on the most fundamental level. Using femtosecond spectroscopy and molecular biology, significant advances have recently been made to map out the entire dynamical evolution and determine actual timescales of all the catalytic processes in photolyases. The repair of CPD reveals seven electron-transfer (ET) reactions among ten elementary steps by a cyclic ET radical mechanism through bifurcating ET pathways, a direct tunneling route mediated by the intervening adenine and a two-step hopping path bridged by the intermediate adenine from the cofactor to damaged DNA, through the conserved folded flavin at the active site. The unified, bifurcated ET mechanism elucidates the molecular origin of various repair quantum yields of different photolyases from three life kingdoms. For 6-4 photoproduct repair, a similar cyclic ET mechanism operates and a new cyclic proton transfer with a conserved histidine residue at the active site of (6-4) photolyases is revealed.
[Mh] Termos MeSH primário: Dano ao DNA
Reparo do DNA
Desoxirribodipirimidina Fotoliase
Flavoproteínas
Dobramento de Proteína
Dímeros de Pirimidina
[Mh] Termos MeSH secundário: Domínio Catalítico
Desoxirribodipirimidina Fotoliase/química
Desoxirribodipirimidina Fotoliase/metabolismo
Transporte de Elétrons
Flavina-Adenina Dinucleotídeo/química
Flavina-Adenina Dinucleotídeo/metabolismo
Flavoproteínas/química
Flavoproteínas/metabolismo
Dímeros de Pirimidina/química
Dímeros de Pirimidina/metabolismo
Raios Ultravioleta
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Flavoproteins); 0 (Pyrimidine Dimers); 146-14-5 (Flavin-Adenine Dinucleotide); EC 4.1.99.3 (Deoxyribodipyrimidine Photo-Lyase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171026
[Lr] Data última revisão:
171026
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170814
[St] Status:MEDLINE


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[PMID]:28735741
[Au] Autor:Britto SM; Shanthakumari D; Agilan B; Radhiga T; Kanimozhi G; Prasad NR
[Ad] Endereço:Department of Biochemistry, Idhaya College of Arts and Science for Women, Pakkamudayanpet, Puducherry 605 008, India; Department of Biochemistry, Research and Development, Bharathiyar University, Coimbatore- 641046, Tamil Nadu, India.
[Ti] Título:Apigenin prevents ultraviolet-B radiation induced cyclobutane pyrimidine dimers formation in human dermal fibroblasts.
[So] Source:Mutat Res;821:28-35, 2017 Sep.
[Is] ISSN:1873-135X
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Exposure to solar ultraviolet-B (UVB) radiation leads to the formation of cyclobutane pyrimidine dimers (CPDs). We investigated the protective effect of apigenin against UVB-induced CPDs formation in human dermal fibroblasts cells (HDFa). For this purpose, HDFa cells were treated with apigenin (15µM) prior to UVB irradiation (20mJ/cm ); DNA damage and subsequent molecular end points were observed. Exposure to UVB radiation increased significant CPDs formation in HDFa cells and the frequencies of CPDs were reduced by treatment with apigenin (15µM). UVB-induced CPDs downregulates the expression of nucleotide excision repair (NER) genes such as xeroderma pigmentosum complementation group C, B, G and F (XPC, XPB, XPG and XPF), transcription factor II human (TFIIH) and excision repair cross-complementation group 1 (ERCC1) in HDFa cells. Conversely, apigenin treatment restored UVB-induced loss of NER proteins in HDFa cells, which indicates its preventive effect against CPDs formation. Besides, single low dose UVB-exposure induced nuclear fragmentation, apoptotic frequency and apoptotic proteins expression (Bax and Caspase-3) have been prevented by the apigenin pretreatment. Furthermore, apigenin exhibits strong UV absorbance property and showed 10.08 SPF value. Thus, apigenin can protect skin cells against UVB-induced CPDs formation probably through its sunscreen effect. Hence, apigenin can be considered as an effective protective agent against UV induced skin damages.
[Mh] Termos MeSH primário: Apigenina/farmacologia
Dano ao DNA
Fibroblastos/efeitos da radiação
Dímeros de Pirimidina/metabolismo
Pele/efeitos da radiação
Protetores Solares/farmacologia
Raios Ultravioleta/efeitos adversos
[Mh] Termos MeSH secundário: Apoptose/genética
Apoptose/efeitos da radiação
Proteínas Reguladoras de Apoptose/genética
Técnicas de Cultura de Células
Linhagem Celular
Ensaio Cometa
Reparo do DNA
Fibroblastos/metabolismo
Fibroblastos/patologia
Seres Humanos
Dose de Radiação
Pele/metabolismo
Pele/patologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Apoptosis Regulatory Proteins); 0 (Pyrimidine Dimers); 0 (Sunscreening Agents); 7V515PI7F6 (Apigenin)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170821
[Lr] Data última revisão:
170821
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170725
[St] Status:MEDLINE


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[PMID]:28642369
[Au] Autor:Nevin P; Gabbai CC; Marians KJ
[Ad] Endereço:From the Molecular Biology Program, Memorial Sloan Kettering Cancer Center, New York, New York 10065.
[Ti] Título:Replisome-mediated translesion synthesis by a cellular replicase.
[So] Source:J Biol Chem;292(33):13833-13842, 2017 Aug 18.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Genome integrity relies on the ability of the replisome to navigate ubiquitous DNA damage during DNA replication. The replisome transiently stalls at leading-strand template lesions and can either reinitiate replication downstream of the lesion or recruit specialized DNA polymerases that can bypass the lesion via translesion synthesis. Previous results had suggested that the replicase might play a role in lesion bypass, but this possibility has not been tested in reconstituted DNA replication systems. We report here that the DNA polymerase III holoenzyme in a stalled replisome can directly bypass a single cyclobutane pyrimidine dimer or abasic site by translesion synthesis in the absence of specialized translesion synthesis polymerases. Bypass efficiency was proportional to deoxynucleotide concentrations equivalent to those found and was dependent on the frequency of primer synthesis downstream of the lesion. Translesion synthesis came at the expense of lesion-skipping replication restart. Replication of a cyclobutane pyrimidine dimer was accurate, whereas replication of an abasic site resulted in mainly -1 frameshifts. Lesion bypass was accompanied by an increase in base substitution frequency for the base preceding the lesion. These findings suggest that DNA damage at the replication fork can be replicated directly by the replisome without the need to activate error-prone pathways.
[Mh] Termos MeSH primário: Quebras de DNA de Cadeia Simples
DNA Polimerase III/metabolismo
Replicação do DNA
DNA Polimerase Dirigida por DNA/metabolismo
Proteínas de Escherichia coli/metabolismo
Escherichia coli/enzimologia
Complexos Multienzimáticos/metabolismo
[Mh] Termos MeSH secundário: DNA Polimerase III/genética
DNA Bacteriano/metabolismo
DNA Polimerase Dirigida por DNA/genética
Escherichia coli/crescimento & desenvolvimento
Escherichia coli/metabolismo
Proteínas de Escherichia coli/genética
Mutação da Fase de Leitura
Furanos/química
Furanos/metabolismo
Holoenzimas/genética
Holoenzimas/metabolismo
Complexos Multienzimáticos/genética
Multimerização Proteica
Dímeros de Pirimidina/química
Dímeros de Pirimidina/metabolismo
Origem de Replicação
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DNA, Bacterial); 0 (Escherichia coli Proteins); 0 (Furans); 0 (Holoenzymes); 0 (Multienzyme Complexes); 0 (Pyrimidine Dimers); 3N8FZZ6PY4 (tetrahydrofuran); EC 2.7.7.- (DNA Polymerase III); EC 2.7.7.- (DNA replicase); EC 2.7.7.- (DNA synthesome); EC 2.7.7.7 (DNA-Directed DNA Polymerase)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170906
[Lr] Data última revisão:
170906
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170624
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M117.800441


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[PMID]:28595074
[Au] Autor:Lee JJ; Kim KB; Heo J; Cho DH; Kim HS; Han SH; Ahn KJ; An IS; An S; Bae S
[Ad] Endereço:Research Institute for Molecular-Targeted Drugs and Department of Cosmetics Engineering, Konkuk University, Seoul 05029, Republic of Korea; Gene Cell Pharm Incorporated, 2nd Enterprise Research Building, Chungcheongbuk-do 28156, Republic of Korea.
[Ti] Título:Protective effect of Arthrospira platensis extracts against ultraviolet B-induced cellular senescence through inhibition of DNA damage and matrix metalloproteinase-1 expression in human dermal fibroblasts.
[So] Source:J Photochem Photobiol B;173:196-203, 2017 Aug.
[Is] ISSN:1873-2682
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:Ultraviolet (UV) light exposure causes skin photoaging, which is known to be preventable and controllable by application of UV-protective agents. In this study, we demonstrated, for the first time, that the extract of microalgae Arthrospira platensis has a reverse effect on UV-induced photodamage such as loss of cell viability, cellular senescence, DNA damage, and collagen destruction in dermal fibroblasts. Forty-eight extracts were prepared from the cell biomass by controlling culture light conditions, extract solvents, and disruption methods. Then, we analyzed their cytotoxicities using WST-1 assay and separated low and high cytotoxic extracts with normal human dermal fibroblasts (nHDFs). Using the low cytotoxic extracts, we performed UVB protection assay and selected the most effective extract demonstrating protective effect against UVB-induced nHDF damage. Flow cytometric analysis and senescence-associated (SA) ß-galactosidase assay showed that pretreatment with the extract reversed UVB-induced G2/M phase cell cycle arrest and senescence in nHDFs. Furthermore, UVB-induced DNA damage in nHDFs, such as cyclobutane pyrimidine dimer formation, was significantly suppressed by the extract. Further, quantitative real-time PCR experiments revealed that the extract significantly inhibited UVB-induced upregulation of matrix metalloproteinase 1 (MMP1) and MMP3 expression in nHDFs. Therefore, we concluded that the microalgae extract can be a potential anti-photoaging agent.
[Mh] Termos MeSH primário: Senescência Celular/efeitos da radiação
Dano ao DNA/efeitos dos fármacos
Metaloproteinase 1 da Matriz/metabolismo
Extratos Vegetais/química
Substâncias Protetoras/farmacologia
Spirulina/química
Raios Ultravioleta
[Mh] Termos MeSH secundário: Sobrevivência Celular/efeitos dos fármacos
Sobrevivência Celular/efeitos da radiação
Células Cultivadas
Senescência Celular/efeitos dos fármacos
Dano ao DNA/efeitos da radiação
Derme/citologia
Fibroblastos/citologia
Fibroblastos/efeitos dos fármacos
Fibroblastos/metabolismo
Pontos de Checagem da Fase G2 do Ciclo Celular/efeitos dos fármacos
Pontos de Checagem da Fase G2 do Ciclo Celular/efeitos da radiação
Seres Humanos
Pontos de Checagem da Fase M do Ciclo Celular/efeitos dos fármacos
Pontos de Checagem da Fase M do Ciclo Celular/efeitos da radiação
Metaloproteinase 1 da Matriz/genética
Extratos Vegetais/farmacologia
Substâncias Protetoras/química
Dímeros de Pirimidina/efeitos da radiação
Spirulina/metabolismo
Regulação para Cima/efeitos dos fármacos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Plant Extracts); 0 (Protective Agents); 0 (Pyrimidine Dimers); EC 3.4.24.7 (Matrix Metalloproteinase 1)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170609
[St] Status:MEDLINE


  9 / 2286 MEDLINE  
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[PMID]:28525579
[Au] Autor:Wang K; Taylor JA
[Ad] Endereço:Department of Chemistry, Washington University, St Louis, MO 63130, USA.
[Ti] Título:Modulation of cyclobutane thymine photodimer formation in T11-tracts in rotationally phased nucleosome core particles and DNA minicircles.
[So] Source:Nucleic Acids Res;45(12):7031-7041, 2017 Jul 07.
[Is] ISSN:1362-4962
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Cyclobutane pyrimidine dimers (CPDs) are DNA photoproducts linked to skin cancer, whose mutagenicity depends in part on their frequency of formation and deamination. Nucleosomes modulate CPD formation, favoring outside facing sites and disfavoring inward facing sites. A similar pattern of CPD formation in protein-free DNA loops suggests that DNA bending causes the modulation in nucleosomes. To systematically study the cause and effect of nucleosome structure on CPD formation and deamination, we have developed a circular permutation synthesis strategy for positioning a target sequence at different superhelix locations (SHLs) across a nucleosome in which the DNA has been rotationally phased with respect to the histone octamer by TG motifs. We have used this system to show that the nucleosome dramatically modulates CPD formation in a T11-tract that covers one full turn of the nucleosome helix at seven different SHLs, and that the position of maximum CPD formation at all locations is shifted to the 5΄-side of that found in mixed-sequence nucleosomes. We also show that an 80-mer minicircle DNA using the same TG-motifs faithfully reproduces the CPD pattern in the nucleosome, indicating that it is a good model for protein-free rotationally phased bent DNA of the same curvature as in a nucleosome, and that bending is modulating CPD formation.
[Mh] Termos MeSH primário: DNA Circular/química
Histonas/química
Nucleossomos/efeitos da radiação
Dímeros de Pirimidina/agonistas
Timina/química
[Mh] Termos MeSH secundário: Animais
Galinhas
DNA Circular/isolamento & purificação
Desaminação
Eritrócitos/química
Histonas/metabolismo
Seres Humanos
Mutagênese
Conformação de Ácido Nucleico
Nucleossomos/química
Nucleossomos/metabolismo
Dímeros de Pirimidina/química
Dímeros de Pirimidina/metabolismo
Timina/metabolismo
Raios Ultravioleta
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DNA, Circular); 0 (Histones); 0 (Nucleosomes); 0 (Pyrimidine Dimers); QR26YLT7LT (Thymine)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171011
[Lr] Data última revisão:
171011
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170520
[St] Status:MEDLINE
[do] DOI:10.1093/nar/gkx427


  10 / 2286 MEDLINE  
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[PMID]:28393477
[Au] Autor:Xu L; Wen B; Wang Y; Tian C; Wu M; Zhu G
[Ad] Endereço:Institute of Molecular Biology and Biotechnology, Anhui Normal University, 1# Beijing East Road, Wuhu, 241000, Anhui, China.
[Ti] Título:Residues at a Single Site Differentiate Animal Cryptochromes from Cyclobutane Pyrimidine Dimer Photolyases by Affecting the Proteins' Preferences for Reduced FAD.
[So] Source:Chembiochem;18(12):1129-1137, 2017 Jun 19.
[Is] ISSN:1439-7633
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Cryptochromes (CRYs) and photolyases belong to the cryptochrome/photolyase family (CPF). Reduced FAD is essential for photolyases to photorepair UV-induced cyclobutane pyrimidine dimers (CPDs) or 6-4 photoproducts in DNA. In Drosophila CRY (dCRY, a type I animal CRY), FAD is converted to the anionic radical but not to the reduced state upon illumination, which might induce a conformational change in the protein to relay the light signal downstream. To explore the foundation of these differences, multiple sequence alignment of 650 CPF protein sequences was performed. We identified a site facing FAD (Ala377 in Escherichia coli CPD photolyase and Val415 in dCRY), hereafter referred to as "site 377", that was distinctly conserved across these sequences: CPD photolyases often had Ala, Ser, or Asn at this site, whereas animal CRYs had Ile, Leu, or Val. The binding affinity for reduced FAD, but not the photorepair activity of E. coli photolyase, was dramatically impaired when replacing Ala377 with any of the three CRY residues. Conversely, in V415S and V415N mutants of dCRY, FAD was photoreduced to its fully reduced state after prolonged illumination, and light-dependent conformational changes of these mutants were severely inhibited. We speculate that the residues at site 377 play a key role in the different preferences of CPF proteins for reduced FAD, which differentiate animal CRYs from CPD photolyases.
[Mh] Termos MeSH primário: Aminoácidos/química
Criptocromos/química
Desoxirribodipirimidina Fotoliase/química
Drosophila melanogaster/metabolismo
Escherichia coli/metabolismo
Flavina-Adenina Dinucleotídeo/química
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Substituição de Aminoácidos
Aminoácidos/metabolismo
Animais
Sítios de Ligação
Clonagem Molecular
Sequência Conservada
Criptocromos/genética
Criptocromos/metabolismo
Desoxirribodipirimidina Fotoliase/genética
Desoxirribodipirimidina Fotoliase/metabolismo
Drosophila melanogaster/genética
Escherichia coli/genética
Flavina-Adenina Dinucleotídeo/metabolismo
Expressão Gênica
Mutação
Oxirredução
Ligação Proteica
Dímeros de Pirimidina/química
Dímeros de Pirimidina/metabolismo
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Especificidade da Espécie
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Amino Acids); 0 (Cryptochromes); 0 (Pyrimidine Dimers); 0 (Recombinant Proteins); 0 (pyrimidine-pyrimidone dimer); 146-14-5 (Flavin-Adenine Dinucleotide); EC 4.1.99.3 (Deoxyribodipyrimidine Photo-Lyase)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170630
[Lr] Data última revisão:
170630
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170411
[St] Status:MEDLINE
[do] DOI:10.1002/cbic.201700145



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